Intracellular signaling regulates a variety of important biological functions. One common method used by cells to conduct signals is protein phosphorylation. In order to transmit signals, activated enzymes called protein kinases attach phosphate groups to downstream molecules in a signaling cascade and thereby, depending on the type of molecule, regulate their enzymatic activity, their subcellular localization, their interaction with other molecules, their shape, or their halflife. One important family of protein kinases involved in this type of signal transmission is the mitogen-activated protein kinases (MAPKs) (Widmann, C. et al., Physiol Rev 79(1):143-80, 1999). Because MAPKs are themselves regulated by phosphorylation, they are often members of complex phosphorelay systems within cells involving other kinases. For example a MAPK can be phosphorylated by MAPK kinases (MKKs), which in turn can be phosphorylated by MAPK kinase kinases (MKKKs). Such a phosphorelay system can serve to amplify a signal, determine the specificity of a signal, and allow regulation at different points in the signaling cascade. MAPKs, MKKs, and MKKKs have been found to play roles in a large variety to cellular activities, including gene expression, mitosis, proliferation, cell movement, metabolism, and programmed cell death. Because of the important functions of protein kinase family enzymes such as the MAPKs, MKKs, and MKKKs, there is a need in the art to identify new MAPK pathway kinases and methods of regulating these new kinases for therapeutic effects.